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Youssef El Khoury, Aurélien Trivella and Petra Hellwig *
Laboratoire de Spectroscopie Vibrationnelle et Electrochimie des Biomolécules Institut de Chimie, UMR 7177, Université de Strasbourg 1 rue Blaise Pascal, 67008 Strasbourg Cedex (France)
* E-mail: hellwig@unistra.fr
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Abstract: Spectroscopic techniques that use the low frequency region are strongly emerging for the study of biological molecules. Far infrared and far Raman spectroscopies, THz time domain approaches and inelastic neutron scattering reveal the presence of vibrational modes involving inter- and intramolecular hydrogen bonding. Due to their collective nature, such modes are highly sensitive to the conformational state of the molecule. Here the influence of the secondary structure on these vibrational features in the far infrared for model compounds and proteins of well known structure are described. Since temperature has a large effect on hydrogen bonding, the development of the signature of poly-L-lysine between 14 and 294 K is presented. The data does not only reveal the increase of the number of hydrogen bonds with temperature, but also the reorganizations within the structures.
Keywords: Far infrared, Hydrogen bonding, Proteins, Polyamino acids, Temperature dependence.
Received: 2010-11-22
Published: 2010-12-31
Cite this article:
Youssef El Khoury, Aur└lien Trivella and Petra Hellwig. (Invited Paper) The Hydrogen Bonding Signature of Peptides and Proteins in the Far Infrared[J]. International Journal of Terahertz Science and Technology, 2010, Vol.3, No.4: 183-191. DOI:10.11906/TST.183-191.2010.12.18
URL: http://www.tstnetwork.org/10.11906/TST.183-191.2010.12.18
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